Supramolecular Modulation of Structural Polymorphism in Pathogenic α-Synuclein Fibrils Using Copper(II) Coordination
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Title
Supramolecular Modulation of Structural Polymorphism in Pathogenic α-Synuclein Fibrils Using Copper(II) Coordination
Authors
Keywords
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Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 57, Issue 12, Pages 3099-3103
Publisher
Wiley
Online
2018-01-25
DOI
10.1002/anie.201712286
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Note: Only part of the references are listed.- Selective imaging of internalized proteopathic α-synuclein seeds in primary neurons reveals mechanistic insight into transmission of synucleinopathies
- (2017) Richard J. Karpowicz et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Molecular Insights into Human Serum Albumin as a Receptor of Amyloid-β in the Extracellular Region
- (2017) Tae Su Choi et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- α-synuclein toxicity in neurodegeneration: mechanism and therapeutic strategies
- (2017) Yvette C Wong et al. NATURE MEDICINE
- Animal models of α-synucleinopathy for Parkinson disease drug development
- (2017) James B. Koprich et al. NATURE REVIEWS NEUROSCIENCE
- Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry
- (2017) Tae Su Choi et al. Scientific Reports
- Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
- (2016) Marcus D Tuttle et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Environmental and genetic factors support the dissociation between α-synuclein aggregation and toxicity
- (2016) Anna Villar-Piqué et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Structure and assembly mechanisms of toxic human islet amyloid polypeptide oligomers associated with copper
- (2016) Shin Jung C. Lee et al. Chemical Science
- Structure-mechanism-based engineering of chemical regulators targeting distinct pathological factors in Alzheimer’s disease
- (2016) Michael W. Beck et al. Nature Communications
- Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
- (2016) Marcus D Tuttle et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Exposure to bacterial endotoxin generates a distinct strain of α-synuclein fibril
- (2016) Changyoun Kim et al. Scientific Reports
- A practical guide to small angle X-ray scattering (SAXS) of flexible and intrinsically disordered proteins
- (2015) Alexey G. Kikhney et al. FEBS LETTERS
- Remote His50 Acts as a Coordination Switch in the High-Affinity N-Terminal Centered Copper(II) Site of α-Synuclein
- (2015) Riccardo De Ricco et al. INORGANIC CHEMISTRY
- Insights on the interaction of alpha-synuclein and metals in the pathophysiology of Parkinson's disease
- (2015) Eleonora Carboni et al. Metallomics
- α-Synuclein strains cause distinct synucleinopathies after local and systemic administration
- (2015) W. Peelaerts et al. NATURE
- Probing Conformational Change of Intrinsically Disordered α-Synuclein to Helical Structures by Distinctive Regional Interactions with Lipid Membranes
- (2014) Shin Jung C. Lee et al. ANALYTICAL CHEMISTRY
- A Revised Picture of the Cu(II)−α-Synuclein Complex: The Role of N-Terminal Acetylation
- (2014) Gina M. Moriarty et al. BIOCHEMISTRY
- Solution conditions determine the relative importance of nucleation and growth processes in -synuclein aggregation
- (2014) A. K. Buell et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Metabolism and functions of copper in brain
- (2014) Ivo F. Scheiber et al. PROGRESS IN NEUROBIOLOGY
- Parkinson's disease dementia: convergence of α-synuclein, tau and amyloid-β pathologies
- (2013) David J. Irwin et al. NATURE REVIEWS NEUROSCIENCE
- Substantia nigra in Parkinson’s disease: a multimodal MRI comparison between early and advanced stages of the disease
- (2013) Domenico Aquino et al. NEUROLOGICAL SCIENCES
- Structural and functional characterization of two alpha-synuclein strains
- (2013) Luc Bousset et al. Nature Communications
- Affinity of copper and zinc ions to proteins and peptides related to neurodegenerative conditions (Aβ, APP, α-synuclein, PrP)
- (2012) Izabela Zawisza et al. COORDINATION CHEMISTRY REVIEWS
- Metal ions and amyloid fiber formation in neurodegenerative diseases. Copper, zinc and iron in Alzheimer's, Parkinson's and prion diseases
- (2012) John H. Viles COORDINATION CHEMISTRY REVIEWS
- Bioinorganic chemistry of copper coordination to alpha-synuclein: Relevance to Parkinson's disease
- (2012) Andrés Binolfi et al. COORDINATION CHEMISTRY REVIEWS
- Localization of copper and copper transporters in the human brain
- (2012) Katherine M. Davies et al. Metallomics
- Coordination Features and Affinity of the Cu2+Site in the α-Synuclein Protein of Parkinson’s Disease
- (2011) Christopher G. Dudzik et al. BIOCHEMISTRY
- Structural characterization of Cu2+, Ni2+ and Zn2+ binding sites of model peptides associated with neurodegenerative diseases
- (2011) Caterina Migliorini et al. COORDINATION CHEMISTRY REVIEWS
- Exogenous α-Synuclein Fibrils Induce Lewy Body Pathology Leading to Synaptic Dysfunction and Neuron Death
- (2011) Laura A. Volpicelli-Daley et al. NEURON
- Copper binding regulates intracellular alpha-synuclein localisation, aggregation and toxicity
- (2010) Xiaoyan Wang et al. JOURNAL OF NEUROCHEMISTRY
- Metalloproteomics and metal toxicology of α-synuclein
- (2010) Aaron Santner et al. Metallomics
- Unique copper-induced oligomers mediate alpha-synuclein toxicity
- (2009) Josephine A. Wright et al. FASEB JOURNAL
- Cu2+Binding Modes of Recombinant α-Synuclein − Insights from EPR Spectroscopy
- (2008) Simon C. Drew et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
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